Weise C, Franke P, Kopácek P, Wiesner A
Institute of Biochemistry, Free University Berlin, Germany.
J Protein Chem. 1998 Oct;17(7):633-41. doi: 10.1007/BF02780964.
The complete amino acid sequence of apolipophorin-III (apoLp-III), a lipid-binding hemolymph protein from the greater wax moth, Galleria mellonella, was determined by protein sequencing. The mature protein consists of 163 amino acid residues forming a protein of 18,075.5 Da. Its sequence is similar to apoLp-III from other Lepidopteran species, but remarkably different from the apoLp-IIIs of insects from other orders. As shown by mass spectrometric analysis, the protein carries no modifications. Thus, all of its known physiological functions, including its recently discovered immune response-stimulating activity, must reside in the protein itself.
通过蛋白质测序确定了大蜡螟(Galleria mellonella)血淋巴中一种脂质结合蛋白——载脂蛋白III(apoLp-III)的完整氨基酸序列。成熟蛋白由163个氨基酸残基组成,形成一种分子量为18,075.5道尔顿的蛋白质。其序列与其他鳞翅目物种的apoLp-III相似,但与其他目昆虫的apoLp-III有显著差异。质谱分析表明,该蛋白没有修饰。因此,其所有已知的生理功能,包括最近发现的免疫反应刺激活性,必定都存在于蛋白质本身。